Results 31 to 40 of about 16,731 (246)

Distribution and Quantitative Estimates of Variant Creutzfeldt-Jakob Disease Prions in Tissues of Clinical and Asymptomatic Patients

open access: yesEmerging Infectious Diseases, 2017
In the United-Kingdom, ≈1 of 2,000 persons could be infected with variant Creutzfeldt-Jakob disease (vCJD). Therefore, risk of transmission of vCJD by medical procedures remains a major concern for public health authorities.
Jean Y. Douet   +11 more
doaj   +1 more source

"Alternative" endocytic mechanisms exploited by pathogens: new avenues for therapeutic delivery? [PDF]

open access: yes, 2007
Some pathogens utilize unique routes to enter cells that may evade the intracellular barriers encountered by the typical clathrin-mediated endocytic pathway.
Medina-Kauwe, LK
core   +1 more source

Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin [PDF]

open access: yesBiochemical Journal, 2008
Disease-related PrPSc [pathogenic PrP (prion protein)] is classically distinguished from its normal cellular precursor, PrPC(cellular PrP) by its detergent insolubility and partial resistance to proteolysis. Although molecular diagnosis of prion disease has historically relied upon detection of protease-resistant fragments of PrPSc using PK (proteinase
Cronier, Sabrina   +6 more
openaire   +4 more sources

Molecular Dynamics Studies on 3D Structures of the Hydrophobic Region PrP(109-136) [PDF]

open access: yes, 2013
Prion diseases caused by the conversion from a soluble normal cellular prion protein into insoluble abnormally folded infectious prions, are invariably fatal and highly infectious degenerative diseases that affect a wide variety of mammalian species. The
Zhang, Jiapu, Zhang, Yuanli
core   +4 more sources

Human Keratinocytes Express Cellular Prion-Related Proteinin Vitro and during Inflammatory Skin Diseases [PDF]

open access: yesThe American Journal of Pathology, 1998
Prion diseases are transmissible spongiform encephalopathies of humans and animals characterized by the accumulation of a proteinase-resistant isoform of the cellular prion-related protein (PrPc) within the central nervous system. In the present report we demonstrate for the first time the presence of PrPc on squamous epithelia of normal and diseased ...
J, Pammer, W, Weninger, E, Tschachler
openaire   +2 more sources

C. elegans Models to Study the Propagation of Prions and Prion-Like Proteins

open access: yesBiomolecules, 2020
A hallmark common to many age-related neurodegenerative diseases, such as Alzheimer’s disease (AD), Parkinson’s disease (PD), and amyotrophic lateral sclerosis (ALS), is that patients develop proteinaceous deposits in their central nervous system (CNS ...
Carl Alexander Sandhof   +3 more
doaj   +1 more source

Antihypertensive drug guanabenz is active in vivo against both yeast and mammalian prions. [PDF]

open access: yesPLoS ONE, 2008
BackgroundPrion-based diseases are incurable transmissible neurodegenerative disorders affecting animals and humans.Methodology/principal findingsHere we report the discovery of the in vivo antiprion activity of Guanabenz (GA), an agonist of alpha2 ...
Déborah Tribouillard-Tanvier   +9 more
doaj   +1 more source

Computational Studies of the Structural Stability of Rabbit Prion Protein Compared to Human and Mouse Prion Proteins [PDF]

open access: yes, 2011
Prion diseases are invariably fatal and highly infectious neurodegenerative diseases affecting humans and animals. The neurodegenerative diseases such as Creutzfeldt-Jakob disease, variant Creutzfeldt-Jakob diseases, Gerstmann-Str$\ddot{a}$ussler ...
Zhang, Jiapu
core   +2 more sources

Prion degradation pathways: Potential for therapeutic intervention [PDF]

open access: yes, 2015
Prion diseases are fatal neurodegenerative disorders. Pathology is closely linked to the misfolding of native cellular PrP(C) into the disease-associated form PrP(Sc) that accumulates in the brain as disease progresses. Although treatments have yet to be
Goold, R, McKinnon, C, Tabrizi, SJ
core   +1 more source

Transgenic Mice Expressing Porcine Prion Protein Resistant to Classical Scrapie but Susceptible to Sheep Bovine Spongiform Encephalopathy and Atypical Scrapie

open access: yesEmerging Infectious Diseases, 2009
How susceptible pigs are to infection with sheep prions is unknown. We show, through transmission experiments in transgenic mice expressing porcine prion protein (PrP), that the susceptibility of this mouse model to bovine spongiform encephalopathy (BSE)
Juan-Carlos Espinosa   +8 more
doaj   +1 more source

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